D. N. Ermolenko, A. V. Zherdev, and B. B. Dzantiev*

Received July 6, 2004
Protein folding is often accompanied by formation of non-native
conformations leading to protein aggregation. A number of reports
indicate that antibodies can facilitate folding and prevent aggregation
of protein antigens. The influence of antibodies on folding is strictly
antigen specific. Chaperone-like antibody activity may be due to the
stabilization of native antigen conformations or folding transition
states, or screening of aggregating hydrophobic surfaces. Taking
advantage of chaperone-like activity of antibodies for immunotherapy
may prove to be a promising approach to the treatment of Alzheimer's
and prion-related diseases. Antibody-assisted folding may enhance
renaturation of recombinant proteins from inclusion bodies.
KEY WORDS: antibodies, protein aggregation, folding, chaperones,
inclusion bodies